20 mM Tris-HCl buffer (pH 8.0) with 10% glycerol, 2 mM DTT, 0.1 M NaCl.
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
0.5 mg/ml (Please refer to the vial label for the specific concentration.)
Full length protein, N-terminal His-Tag; MGSSHHHHHH SSGLVPRGSH MGSMWNSGFE SYGSSSYGGA GGYTQSPGGF GSPAPSQAEK KSRARAQHIV PCTISQLLSA TLVDEVFRIG NVEISQVTIV GIIRHAEKAP TNIVYKIDDM TAAPMDVRQW VDTDDTSSEN TVVPPETYVK VAGHLRSFQN KKSLVAFKIM PLEDMNEFTT HILEVINAHM VLSKANSQPS AGRAPISNPG MSEAGNFGGN SFMPANGLTV AQNQVLNLIK ACPRPEGLNF QDLKNQLKHM SVSSIKQAVD FLSNEGHIYS TVDDDHFKST DAE
> 85% by SDS-PAGE.
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
replication protein A2 , REPA2 , RP-A p32 , RP-A p34 , RPA32
This gene encodes a subunit of the heterotrimeric Replication Protein A (RPA) complex, which binds to single-stranded DNA (ssDNA), forming a nucleoprotein complex that plays an important role in DNA metabolism, being involved in DNA replication, repair, recombination, telomere maintenance, and co-ordinating the cellular response to DNA damage through activation of the ataxia telangiectasia and Rad3-related protein (ATR) kinase. The RPA complex protects single-stranded DNA from nucleases, prevents formation of secondary structures that would interfere with repair, and co-ordinates the recruitment and departure of different genome maintenance factors. The heterotrimeric complex has two different modes of ssDNA binding, a low-affinity and high-affinity mode, determined by which oligonucleotide/oligosaccharide-binding (OB) domains of the complex are utilized, and differing in the length of DNA bound. This subunit contains a single OB domain that participates in high-affinity DNA binding and also contains a winged helix domain at its carboxy terminus, which interacts with many genome maintenance protein. Post-translational modifications of the RPA complex also plays a role in co-ordinating different damage response pathways. [provided by RefSeq, Sep 2017]